ID Q4L0H5_BOVIN Unreviewed; 362 AA. AC Q4L0H5; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 24-JAN-2024, entry version 74. DE RecName: Full=2'-5' oligoadenylate synthase {ECO:0000256|ARBA:ARBA00012577}; DE EC=2.7.7.84 {ECO:0000256|ARBA:ARBA00012577}; GN Name=oas1z {ECO:0000313|EMBL:AAT70234.1}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAT70234.1}; RN [1] {ECO:0000313|EMBL:AAT70234.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17024523; DOI=10.1007/s00239-006-0073-3; RA Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.; RT "The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for RT concerted evolution of paralogous Oas1 genes in Rodentia and RT Artiodactyla."; RL J. Mol. Evol. 63:562-576(2006). CC -!- CATALYTIC ACTIVITY: CC Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')- CC adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84; CC Evidence={ECO:0000256|ARBA:ARBA00001112}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the 2-5A synthase family. CC {ECO:0000256|ARBA:ARBA00009526}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY650038; AAT70234.1; -; mRNA. DR RefSeq; NP_001025017.1; NM_001029846.1. DR AlphaFoldDB; Q4L0H5; -. DR GeneID; 519922; -. DR KEGG; bta:519922; -. DR CTD; 519922; -. DR OrthoDB; 4638494at2759; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IEA:UniProtKB-EC. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1. DR Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C. DR InterPro; IPR006117; 2-5OAS_C_CS. DR InterPro; IPR043518; 2-5OAS_N_CS. DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR PANTHER; PTHR11258:SF13; 2'-5'-OLIGOADENYLATE SYNTHASE 1; 1. DR PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1. DR Pfam; PF01909; NTP_transf_2; 1. DR Pfam; PF10421; OAS1_C; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1. DR PROSITE; PS00832; 25A_SYNTH_1; 1. DR PROSITE; PS00833; 25A_SYNTH_2; 1. DR PROSITE; PS50152; 25A_SYNTH_3; 1. PE 2: Evidence at transcript level; KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Immunity {ECO:0000256|ARBA:ARBA00022859}; KW Innate immunity {ECO:0000256|ARBA:ARBA00022588}. FT DOMAIN 38..106 FT /note="Polymerase nucleotidyl transferase" FT /evidence="ECO:0000259|Pfam:PF01909" FT DOMAIN 164..348 FT /note="2'-5'-oligoadenylate synthetase 1" FT /evidence="ECO:0000259|Pfam:PF10421" SQ SEQUENCE 362 AA; 42696 MW; 1D137C94D2EB4A47 CRC64; MKKLRKTQAN KLDKFIKDHL LPHEEFQRQV NEAIDIICTF LKETCFQEST HPVRVSKVVK GGSSGKGTTL KDLSDADLVV FLTNLTSFQE NFEHRVRFIK EIRRQLEAYQ RQKTFEVEFE VLKQRKRKRR ALSFVLRSPW FCQGVKFDVL PAFDALAQVT EDYKPNPQIY VQLIQECENL RREGEFSPCF TELQRAFLKE RPAKLKSLIR LVKHWYQQCK KRHGKKLPSQ YALELLTIYA WEQEGSKTKF RTAEGFRTVL ELVLKHQDLC IYWKKYYDFE NPIITQCLKR QLEKPRPVIL DPADPTGNVA GREPQRWQLL AQEVTVWLRY SCCKNWNGSP VSPWNVPVTP PHYLSDLILM AC //